Document Detail

Structure of the catalytic fragment of poly(AD-ribose) polymerase from chicken.
MedLine Citation:
PMID:  8755499     Owner:  NLM     Status:  MEDLINE    
The crystal structures of the catalytic fragment of chicken poly(ADP-ribose) polymerase [NAD+ ADP-ribosyltransferase; NAD+:poly(adenosine-diphosphate-D-ribosyl)-acceptor ADP-D-ribosyltransferase, EC] with and without a nicotinamide-analogue inhibitor have been elucidated. Because this enzyme is involved in the regulation of DNA repair, its inhibitors are of interest for cancer therapy. The inhibitor shows the nicotinamide site and also suggests the adenosine site. The enzyme is structurally related to bacterial ADP-ribosylating toxins but contains an additional alpha-helical domain that is suggested to relay the activation signal issued on binding to damaged DNA.
A Ruf; J Mennissier de Murcia; G de Murcia; G E Schulz
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Proceedings of the National Academy of Sciences of the United States of America     Volume:  93     ISSN:  0027-8424     ISO Abbreviation:  Proc. Natl. Acad. Sci. U.S.A.     Publication Date:  1996 Jul 
Date Detail:
Created Date:  1996-10-29     Completed Date:  1996-10-29     Revised Date:  2009-11-18    
Medline Journal Info:
Nlm Unique ID:  7505876     Medline TA:  Proc Natl Acad Sci U S A     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  7481-5     Citation Subset:  IM    
Institut für Organische Chemie und Biochemie, Freiburg im Breisgau, Germany.
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MeSH Terms
Binding Sites
Cell Line
Crystallography, X-Ray
DNA Damage
DNA Repair
Models, Molecular
Molecular Sequence Data
NAD / metabolism*
Peptide Fragments / biosynthesis,  chemistry*
Poly(ADP-ribose) Polymerases / biosynthesis,  chemistry*
Protein Structure, Secondary*
Recombinant Proteins / biosynthesis,  chemistry
Reg. No./Substance:
0/Peptide Fragments; 0/Recombinant Proteins; 53-84-9/NAD; EC Polymerases

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

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